Modification of nonstructural protein 1 of influenza A virus by SUMO1.
Identifieur interne : 000208 ( Hal/Curation ); précédent : 000207; suivant : 000209Modification of nonstructural protein 1 of influenza A virus by SUMO1.
Auteurs : Ke Xu [République populaire de Chine] ; Christoph Klenk [Allemagne] ; Bin Liu [République populaire de Chine] ; Bjoern Keiner [Allemagne] ; Jinke Cheng [République populaire de Chine] ; Bo-Jian Zheng [République populaire de Chine] ; Li Li [République populaire de Chine] ; Qinglin Han [République populaire de Chine] ; Chen Wang [République populaire de Chine] ; Tianxian Li [République populaire de Chine] ; Ze Chen [République populaire de Chine] ; Yuelong Shu [République populaire de Chine] ; Jinhua Liu [République populaire de Chine] ; Hans-Dieter Klenk [Allemagne] ; Bing Sun [République populaire de Chine]Source :
- Journal of Virology [ 0022-538X ] ; 2011-01.
Abstract
Nonstructural protein 1 (NS1) is one of the major factors resulting in the efficient infection rate and high level of virulence of influenza A virus. Although consisting of only approximately 230 amino acids, NS1 has the ability to interfere with several systems of the host viral defense. In the present study, we demonstrate that NS1 of the highly pathogenic avian influenza A/Duck/Hubei/L-1/2004 (H5N1) virus interacts with human Ubc9, which is the E2 conjugating enzyme for sumoylation, and we show that SUMO1 is conjugated to H5N1 NS1 in both transfected and infected cells. Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites. When the SUMO1 acceptor sites were removed by mutation, NS1 underwent rapid degradation. Studies of different influenza A virus strains of human and avian origin showed that the majority of viruses possess an NS1 protein that is modified by SUMO1, except for the recently emerged swine-origin influenza A virus (S-OIV) (H1N1). Interestingly, growth of a sumoylation-deficient WSN virus mutant was retarded compared to that of wild-type virus. Together, these results indicate that sumoylation enhances NS1 stability and thus promotes rapid growth of influenza A virus.
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DOI: 10.1128/JVI.00877-10
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<idno type="DOI">10.1128/JVI.00877-10</idno>
<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date type="datePub">2011-01</date>
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<front><div type="abstract" xml:lang="en"> <p>Nonstructural protein 1 (NS1) is one of the major factors resulting in the efficient infection rate and high level of virulence of influenza A virus. Although consisting of only approximately 230 amino acids, NS1 has the ability to interfere with several systems of the host viral defense. In the present study, we demonstrate that NS1 of the highly pathogenic avian influenza A/Duck/Hubei/L-1/2004 (H5N1) virus interacts with human Ubc9, which is the E2 conjugating enzyme for sumoylation, and we show that SUMO1 is conjugated to H5N1 NS1 in both transfected and infected cells. Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites. When the SUMO1 acceptor sites were removed by mutation, NS1 underwent rapid degradation. Studies of different influenza A virus strains of human and avian origin showed that the majority of viruses possess an NS1 protein that is modified by SUMO1, except for the recently emerged swine-origin influenza A virus (S-OIV) (H1N1). Interestingly, growth of a sumoylation-deficient WSN virus mutant was retarded compared to that of wild-type virus. Together, these results indicate that sumoylation enhances NS1 stability and thus promotes rapid growth of influenza A virus.</p>
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<hal api="V3"> <titleStmt> <title xml:lang="en">Modification of nonstructural protein 1 of influenza A virus by SUMO1.</title>
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</author>
<author role="aut"> <persName> <forename type="first">Bjoern</forename>
<surname>Keiner</surname>
</persName>
<idno type="halauthorid">643685</idno>
<affiliation ref="#struct-221820"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Jinke</forename>
<surname>Cheng</surname>
</persName>
<idno type="halauthorid">643956</idno>
<affiliation ref="#struct-169901"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Bo-Jian</forename>
<surname>Zheng</surname>
</persName>
<idno type="halauthorid">639000</idno>
<affiliation ref="#struct-136023"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Li</forename>
<surname>Li</surname>
</persName>
<idno type="halauthorid">105104</idno>
<affiliation ref="#struct-168263"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Qinglin</forename>
<surname>Han</surname>
</persName>
<idno type="halauthorid">643957</idno>
<affiliation ref="#struct-168263"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Chen</forename>
<surname>Wang</surname>
</persName>
<idno type="halauthorid">219411</idno>
<affiliation ref="#struct-169903"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Tianxian</forename>
<surname>Li</surname>
</persName>
<idno type="halauthorid">643688</idno>
<affiliation ref="#struct-169904"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Ze</forename>
<surname>Chen</surname>
</persName>
<idno type="halauthorid">641724</idno>
<affiliation ref="#struct-169905"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Yuelong</forename>
<surname>Shu</surname>
</persName>
<idno type="halauthorid">643958</idno>
<affiliation ref="#struct-222141"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Jinhua</forename>
<surname>Liu</surname>
</persName>
<idno type="halauthorid">643689</idno>
<affiliation ref="#struct-169907"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Hans-Dieter</forename>
<surname>Klenk</surname>
</persName>
<idno type="halauthorid">129057</idno>
<affiliation ref="#struct-221820"></affiliation>
</author>
<author role="crp"> <persName> <forename type="first">Bing</forename>
<surname>Sun</surname>
</persName>
<email type="md5">e7f27f228915ea81207e91cbf72c8044</email>
<email type="domain">sibs.ac.cn</email>
<idno type="halauthorid">641725</idno>
<affiliation ref="#struct-168263"></affiliation>
<affiliation ref="#struct-168889"></affiliation>
</author>
</analytic>
<monogr> <idno type="halJournalId" status="VALID">6614</idno>
<idno type="issn">0022-538X</idno>
<idno type="eissn">1098-5514</idno>
<title level="j">Journal of Virology</title>
<imprint> <publisher>American Society for Microbiology</publisher>
<biblScope unit="volume">85</biblScope>
<biblScope unit="issue">2</biblScope>
<biblScope unit="pp">1086-98</biblScope>
<date type="datePub">2011-01</date>
<date type="dateEpub">2010-11-03</date>
</imprint>
</monogr>
<idno type="doi">10.1128/JVI.00877-10</idno>
<idno type="pubmed">21047957</idno>
</biblStruct>
</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <classCode scheme="mesh">Animals</classCode>
<classCode scheme="mesh">Cell Line</classCode>
<classCode scheme="mesh">Mutagenesis, Site-Directed</classCode>
<classCode scheme="mesh">Protein Binding</classCode>
<classCode scheme="mesh">SUMO-1 Protein</classCode>
<classCode scheme="mesh">Sumoylation</classCode>
<classCode scheme="mesh">Two-Hybrid System Techniques</classCode>
<classCode scheme="mesh">Ubiquitin-Conjugating Enzymes</classCode>
<classCode scheme="mesh">Viral Nonstructural Proteins</classCode>
<classCode scheme="mesh">Virulence</classCode>
<classCode scheme="mesh">Dogs</classCode>
<classCode scheme="mesh">Host-Pathogen Interactions</classCode>
<classCode scheme="mesh">Humans</classCode>
<classCode scheme="mesh">Immunohistochemistry</classCode>
<classCode scheme="mesh">Influenza A Virus, H1N1 Subtype</classCode>
<classCode scheme="mesh">Influenza A Virus, H5N1 Subtype</classCode>
<classCode scheme="mesh">Lysine</classCode>
<classCode scheme="mesh">Microscopy, Confocal</classCode>
<classCode scheme="halDomain" n="sdv.mp">Life Sciences [q-bio]/Microbiology and Parasitology</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en"> <p>Nonstructural protein 1 (NS1) is one of the major factors resulting in the efficient infection rate and high level of virulence of influenza A virus. Although consisting of only approximately 230 amino acids, NS1 has the ability to interfere with several systems of the host viral defense. In the present study, we demonstrate that NS1 of the highly pathogenic avian influenza A/Duck/Hubei/L-1/2004 (H5N1) virus interacts with human Ubc9, which is the E2 conjugating enzyme for sumoylation, and we show that SUMO1 is conjugated to H5N1 NS1 in both transfected and infected cells. Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites. When the SUMO1 acceptor sites were removed by mutation, NS1 underwent rapid degradation. Studies of different influenza A virus strains of human and avian origin showed that the majority of viruses possess an NS1 protein that is modified by SUMO1, except for the recently emerged swine-origin influenza A virus (S-OIV) (H1N1). Interestingly, growth of a sumoylation-deficient WSN virus mutant was retarded compared to that of wild-type virus. Together, these results indicate that sumoylation enhances NS1 stability and thus promotes rapid growth of influenza A virus.</p>
</abstract>
</profileDesc>
</hal>
</record>
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